Inhibitors of the catalytic domain of mitochondrial ATP synthase.
Biochem Soc Trans, 2006/11;34(Pt 5):989-92.
Gledhill JR[1], Walker JE
Affiliations
PMID: 17052243
Impact factor: 4.919
Abstract
An understanding of the mechanism of ATP synthase requires an explanation of how inhibitors act. The catalytic F1-ATPase domain of the enzyme has been studied extensively by X-ray crystallography in a variety of inhibited states. Four independent inhibitory sites have been identified by high-resolution structural studies. They are the catalytic site, and the binding sites for the antibiotics aurovertin and efrapeptin and for the natural inhibitor protein, IF1.
MeSH terms
Catalytic Domain; Dicyclohexylcarbodiimide; Enzyme Inhibitors; Mitochondrial Proton-Translocating ATPases; Models, Molecular; Protein Conformation
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